ID A0A194URB1_9PEZI Unreviewed; 1059 AA.
AC A0A194URB1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carboxylic acid reductase {ECO:0000313|EMBL:KUI54166.1};
GN ORFNames=VP1G_01657 {ECO:0000313|EMBL:KUI54166.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI54166.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN714672; KUI54166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194URB1; -.
DR STRING; 694573.A0A194URB1; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT DOMAIN 562..645
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1059 AA; 117639 MW; 1BC5F1BED6EC0CFE CRC64;
MGSVANSENV PYGKRLLPHI VDEVASKDPN RECIQIPWSS EPSDGWRTIT WKDVANGINR
CAHRIVELFG TPQEGSFPTI AYIGPNDARY VLMMIAASKA GYKALFISPR NSKEGQINLF
KTTDCNILAF ASSHKDTIKP WIAEHSMQTF EVSPLDSWFP DTEVPHFTYT KTFEDAEWDP
LLVLHTSGST GLPKPIIVKQ GMWAGMDAYH NLPKFEGKNV AMREWAERAK RHFIPMPLFH
IAGLLCVVNL SLYFDTPVAL GIPDRPLSAD NVIECLENLD VESAFLPPAV IEDMSQTDEG
TKALTSLNVV AFGGGNLARE AGNRLVKQGA VFMNLIGSTE FAPFPTYARN DPEAWQYFVY
NPNVMGCEFR KQGDEDVYEM VVVRQNKHPG LQGIFYTFPE LNEWSSRDLY RPHPTKPYHW
IYHGRADNII VFSNGEKLNP VTIEEIVSDH PCLKGALVVG SEKFQAGLII EPYEDPKNAA
EEQALLDSVW PLVERANEET VAHGRISRDM IRLSNPQKPF LRAAKGTVQR AGTIKLYADE
IEKLYEKESS DQDEDAPKLD ISSEDALTAS IVDALRKDVG ADKLDADVDF FAAGIDSLGV
MRAAKLLRAG LKEAGHEVDA KSFATRVIYQ NSTPRRLARH ILNAFINGQG ESLSEDEQQI
QAMEVIWNKY TSNLTKAVPN RPDPNTKDQT VILTGSTGML GSYLLDFMGR NPRVSKIICF
NRAADGGRAQ GLKACAERGL DATALKTKAE FYQVDLSQPK LGLSDEVYAR LQAETDRVIH
NAWPVNFNIP IESFDPSLAG VRHIADLAAT AAKRVAVTFI ASIAVADRWQ EEGKVPETRL
EELALANGGY GRSKMVGSLI LEDAAAKGAG DFPYAIVRVG QIAGPEGEAG EWNKHEWLPS
IIASSLYLHA LPKNLGTMDR VDWTPVERVA KLVLEASGTA RVVQSADEIN GYYHGVNPNY
TQWYDLALAV QEFYGKDKIP EFISFSEWVD RLEKSQADGP ESVAANPGVK LIDTYRAMAS
ADKAVVYDME KTLERCPVVK ETKAITPEMM KHWCAQWRH
//